Identification of bovine sperm acrosomal proteins that interact with a 32-kDa acrosomal matrix protein

Molecular and Cellular Biochemistry
Subir K NagDasSamir Raychoudhury

Abstract

Mammalian fertilization is accomplished by the interaction between sperm and egg. Previous studies from this laboratory have identified a stable acrosomal matrix assembly from the bovine sperm acrosome termed the outer acrosomal membrane-matrix complex (OMC). This stable matrix assembly exhibits precise binding activity for acrosin and N-acetylglucosaminidase. A highly purified OMC fraction comprises three major (54, 50, and 45 kDa) and several minor (38-19 kDa) polypeptides. The set of minor polypeptides (38-19 kDa) termed "OMCrpf polypeptides" is selectively solubilized by high-pH extraction (pH 10.5), while the three major polypeptides (55, 50, and 45 kDa) remain insoluble. Proteomic identification of the OMC32 polypeptide (32 kDa polypeptide isolated from high-pH soluble fraction of OMC) yielded two peptides that matched the NCBI database sequence of acrosin-binding protein. Anti-OMC32 recognized an antigenically related family of polypeptides (OMCrpf polypeptides) in the 38-19-kDa range with isoelectric points ranging between 4.0 and 5.1. Other than glycohydrolases, OMC32 may also be complexed to other acrosomal proteins. The present study was undertaken to identify and localize the OMC32 binding polypeptides and to elucid...Continue Reading

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Citations

Nov 9, 2016·Journal of Reproductive Immunology·Ganapathy Narmadha, Suresh Yenugu
Mar 31, 2017·Reproduction : the Official Journal of the Society for the Study of Fertility·Wan-Sheng LiuMichael O'Connor
Feb 5, 2019·Reproduction, Fertility, and Development·Peng ZhangLiqing Fan
Aug 31, 2019·Scientific Reports·Michal ZigoPeter Sutovsky
May 7, 2021·Biopreservation and Biobanking·Gul Ipek Gundogan, Abit Aktas

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